分子动力学模拟研究NCBD与TAD相互作用的构象变化

The Analysis of Conformational Changes by Using Molecular Dynamic Simulations Between NCBD and TAD

P53是固有无序蛋白,在细胞信号转导网络中,起着非常重要的作用,它能引导细胞的降解死亡等.P53和CBP是多位点结合,其中P53的TAD的结构域与CBP的NCBD结构域之间的结合,对P53与DNA形成四聚体起到关键的作用.对apo-TAD,apo-NCBD和复合物进行了500ns分子动力学模拟,分析了三个体系的Cα原子的均方根偏差(RMSD)和均方根涨落(RMSF)以及回旋半径(Rg).分析结果表明复合物比apo-TAD和apo-NCBD单体更稳定,尤其是结合位点附近的残基.

P53,which is an intrinsic disordered protein,plays a very important role in cellular signal transduction network,it can direct the degradation of cell and so on.There are multiply binding site between P53 and CBP.The interaction between the nuclear coactivator binding domain（NCBD）of cyclic-AMP response element binding protein（CBP）and the transactivation domain（TAD）of p53 plays an important role in the forming of tetramers.Three 500 ns MD simulations were performed.The Root Mean Square Deviation（RMSDs）,Root Mean Square Fluctuation（RMSFs）and Radius of Gyration（Rgs）of Cαatoms were analyzed for three systems.The results show that the complex are more stable than the apoTAD or apo-NCBD,especially for the residue around the binding.